SQT1, which encodes an essential WD domain protein of saccharomyces cerevisiae, suppresses dominant-negative mutations of the ribosomal protein gene QSR1

Molecular and Cellular Biology

Volumn 17, Issue 9, 1997, Pages 5146-5155

  Eisinger, Dominic P ^a,b   Dick, Frederick A ^a   Denke, Elke ^a   Trumpower, Bernard L ^a  

^a DARTMOUTH MEDICAL SCHOOL   (United States)

^b Adirondack Biomedical Research Institute Inc   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

RIBOSOME PROTEIN;

ARTICLE; FUNGUS GROWTH; GENE FUNCTION; GENE MUTATION; GENE REPRESSION; NONHUMAN; POLYSOME; PRIORITY JOURNAL; PROTEIN DOMAIN; SACCHAROMYCES CEREVISIAE;

EUKARYOTA; FUNGI; SACCHAROMYCES CEREVISIAE;

EID: 0030835426     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.17.9.5146     Document Type: Article

References (60)

1. Ausubel, F. M., R. E. Brent, D. D. Moore, J. A. Smith, J. G. Seidman, and K. Struhl. 1996. Current protocols in molecular biology. Wiley Interscience, New York, N.Y.
2. Ballesta, J. P., and M. Remacha. 1996. The large ribosomal subunit stalk as a regulatory element of the eukaryotic translational machinery. Prog. Nucleic Acids Res. Mol. Biol. 55:157-193.
3. Baudin, A., O. Ozier-Kalogeropoulos, A. Denouel, F. Lacroute, and C. Cullin. 1993. A simple and efficient method for direct gene deletion in Saccharomyces cerevisiae. Nucleic Acids Res. 21:3329-3330.
4. Beckner, M. E., H. C. Krutzsch, M. L. Stracke, S. T. Williams, J. A. Gallardo, and L. A. Liotta. 1995. Identification of a new immunoglobulin superfamily protein expressed in blood vessels with a heparin-binding consensus sequence. Cancer Res. 55:2140-2149.
5. Bonneaud, N., O. Ozier-Kalogeropoulos, G. Li, M. Labouesse, L. Minivielle-Sebastia, and F. Lacroute. 1991. A family of low and high copy replicative, integrative and single-stranded S. cerevisiae/E. coli shuttle vectors. Yeast 7:609-615.
6. Borgese, N. 1974. Ribosomal-membrane interaction: in vitro binding of ribosomes to microsomal membranes. J. Mol. Biol. 88:559-580.
7. Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principal of protein-dye binding. Anal. Biochem. 72:248-254.
8. Chakravarti, D., and U. Maitra. 1993. Eukaryotic initiation factor 5 from Saccharomyces cerevisiae. J. Biol. Chem. 268:10524-10533.
9. Chan, Y., J. Diaz, L. Denoroy, J. Madjar, and I. G. Wool. 1996. The primary structure of rat ribosomal protein L10: relationship to a Jun-binding protein and to a putative Wilms' tumor suppressor. Biochem. Biophys. Res. Commun. 225:952-956.
10. Cigan, M. A., M. Foiani, E. M. Hannig, and A. G. Hinnebusch. 1991. Complex formation by positive and negative translational regulators of GCN4. Mol. Cell. Biol. 11:3217-3228.
11. Deshmukh, M., J. Stark, L. C. Yeh, J. C. Lee, and J. L. Woolford. 1995. Multiple regions of the yeast ribosomal protein L1 are important for its interaction with 5S rRNA and assembly into ribosomes. J. Biol. Chem. 270:30148-30156.
12. Deshmukh, M., Y. Tsay, A. G. Paulovich, and J. L. Woolford. 1993. Depletion of Saccharomyces cerevisiae ribosomal protein L16 causes a decrease in 60S ribosomal subunits and formation of half-mer polyribosomes. Mol. Cell. Biol. 13:2835-2845.
13. 1 complex, codes for a 60S ribosomal subunit protein. J. Biol. Chem. 272:13372-13379.
14. Eisinger, D. P., F. A. Dick, and B. L. Trumpower. 1997. Qsr1p, a 60S ribosomal subunit protein, is required for joining of 40S and 60S subunits. Mol. Cell. Biol. 17:5136-5145.
15. Eisinger, D. P., and B. L. Trumpower. Long-inverse PCR to generate regional peptide libraries by codon mutagenesis. BioTechniques, in press.
16. Farmer, A. A., T. M. Loftus, A. A. Mills, K. Y. Sato, J. D. Neil, T. Tron, M. Yang, B. L. Trumpower, and E. J. Stanbridge. 1994. Extreme evolutionary conservation of QM, a novel c-Jun associated transcription factor. Hum. Mol. Genet. 3:723-728.
17. Fields, S., and O. Song. 1989. A novel genetic system to detect protein-protein interactions. Nature (London) 340:245-246.
18. Fioani, M., M. A. Cigan, C. J. Paddon, S. Harashima, and A. G. Hinnebusch. 1991. GCD2, a translational repressor of the GCN4 gene, has a general function in the initiation of protein synthesis in Saccharomyces cerevisiae. Mol. Cell. Biol. 11:3203-3216.
19. Garcia-Barrio, M. T., T. Naranda, C. R. Vazquez de Aldana, R. Cuesta, A. G. Hinnebusch, J. W. B. Hershey, and M. Tamame. 1995. GCD10, a translational repressor of GCN4, is the RNA-binding subunit of eukaryotic translation initiation faclor-3. Genes Dev. 15:1781-1796.
20. Gyuris, J., E. Golemis, H. Chertkov, and R. Brent. 1993. Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2. Cell 75:791-803.
21. Hanahan, D. 1985. Techniques for transformation of E. coli, p. 115. In D. M. Glover (ed.), DNA cloning - a practical approach, vol. 1. IRL Press, Oxford, United Kingdom.
22. Harper, J. W., G. R. Adami, N. Wei, K. Keyomarsi, and S. J. Elledge. 1993. The p21 Cdk-interaction protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases. Cell 75:805-816.
23. Helser, T., R. Baan, and A. Dahlberg. 1981. Characterization of a 40S ribosomal subunit complex in polyribosomes of Saccharomyces cerevisiae treated with cycloheximide. Mol. Cell. Biol. 1:51-57.
24. Hershey, J. W. B., and M. C. Merrick. 1996. The pathway and mechanism of eukaryotic protein synthesis, p. 31-69. In J. W. B. Hershey, M. B. Mathews, and N. Sonenberg (ed.), Translational control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
25. Herskowitz, I. 1987. Functional inactivation of genes by dominant-negative mutations. Nature 329:219-222.
26. Hinnebusch, A. G. 1994. Translational control of GCN4: an in vivo barometer of initiation-factor activity. Trends Biochem. Sci. 19:409-414.
27. Houman, F., and C. Holm. 1994. DBF8, an essential gene required for efficient chromosome segregation in Saccharomyces cerevisiae. Mol. Cell. Biol. 14:6350-6360.
28. Ju, Q., and J. R. Warner. 1994. Ribosome synthesis during the growth cycle of Saccharomyces cerevisiae. Yeast 10:151-157.
29. Kalies, K. U., D. Gorlich, and T. A. Rapoport. 1994. Binding of ribosomes to the rough endoplasmic reticulum mediated by the Sec61p-complex. J. Cell Biol. 126:925-934.
30. Keleher, C. A., M. J. Red, J. Schultz, M. Carlson, and A. D. Johnson. 1992. SSN6-Tup1 is a general repressor of transcription in yeast. Cell 68:709-719.
31. Kolodziej, P. A., and R. A. Young. 1991. Epitope tagging and protein surveillance. Methods Enzymol. 194:508-519.
32. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
33. Lamphear, B. J., R. Kirchwegar, T. Skern, and R. E. Rhoads. 1995. Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornavirus proteases. J. Biol. Chem. 270:21975-21983.
34. Manivasakam, P., S. C. Weber, J. McElver, and R. H. Schiestl. 1995. Microhomology mediated PCR targeting in Saccharomyces cerevisiae. Nucleic Acids Res. 23:2799-2800.
35. - mRNA surveillance by a yeast antiviral system. Mol. Cell. Biol. 15:2763-2771.
36. Melese, T., and Z. Xue. 1995. The nucleolus: an organelle formed by the act of building a ribosome. Curr. Opin. Cell Biol. 7:319-324.
37. Miller, J. H. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
38. Moritz, M., A. G. Paulovich, Y. F. Tsay, and J. L. Woolford, Jr. 1990. Depletion of yeast ribosomal proteins L16 or rp59 disrupts ribosome assembly. J. Cell Biol. 111:2261-2274.
39. Moritz, M., B. A. Pulaski, and J. L. Woolford, Jr. 1991. Assembly of 60S ribosomal subunits is perturbed in temperature-sensitive yeast mutants defective in ribosomal protein L16. Mol. Cell. Biol. 11:5681-5692.
40. Naranda, T., M. Kainuma, S. E. MacMillan, and J. W. B. Hershey. 1997. The 39-kilodalton subunit of eukaryotic translation initiation factor 3 is essential for the complex's integrity and for cell viability in Saccharomyces cerevisiae. Mol. Cell. Biol. 17:145-153.
41. Naranda, T. S., E. MacMillan, and J. W. B. Hershey. 1994. Purified yeast translational initiation factor eIF-3 is an RNA-binding protein complex that contains the PRT1 protein. J. Biol. Chem. 269:32286-32292.
42. Naranda, T. S., E. MacMillan, T. F. Donahue, and J. W. B. Hershey. 1996. SUI1/p16 is required for the activity of eukaryotic translation initiation factor 3 in Saccharomyces cerevisiae. Mol. Cell. Biol. 16:2307-2313.
43. Naysmith, K. A., and K. Tatchell. 1980. The structure of the transposable yeast mating type loci. Cell 19:753-764.
44. Neer, E. J., C. J. Schmidt, R. Nambudripad, and T. F. Smith. 1994. The ancient regulatory-protein family of WD-repeat proteins. Nature 371:297-300.
45. Ohtake, Y., and R. B. Wickner. 1995. Yeast virus propagation depends critically on free 60S ribosomal subunit concentration. Mol. Cell. Biol. 15: 2772-2781.
46. Ramirez, M., R. C. Wek, and A. G. Hinnebusch. 1991. Ribosome association of GCN2 protein kinase, a translational activator of the GCN4 gene of Saccharomvces cerevisiae. Mol. Cell. Biol. 11:3027-3036.
47. Rotenberg, M. O., M. Moritz, and J. L. Woolford. 1988. Depletion of Saccharomyces cerevisiae ribosomal protein L16 causes a decrease in 60S ribosomal subunits and formation of half-mer polyribosomes. Genes Dev. 2:160-172.
48. Sachs, A. B., and R. W. Davis. 1989. The poly(A) binding protein is required for poly(A) shortening and 60S ribosomal subunit-dependent translation initiation. Cell 58:857-867.
49. Sikorski, R. S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulations of DNA in Saccharomyces cerevisiae. Genetics 122:19-27.
50. Sonenberg, N. 1996. mRNA 5′ cap-binding protein eIF4E and control of cell growth, p. 245-269. In J. W. B. Hershey, M. B. Mathews, and N. Sonenberg (ed.), Translational control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
51. Struhl, K. 1987. Promoters, activator proteins, and the mechanism of transcriptional initiation in yeast. Cell 49:295-297.
52. Tollervey, D., H. Lehtonen, R. Jansen, H. Kern, and E. C. Hurt. 1993. Temperature-sensitive mutations demonstrate roles for yeast fibrillarin in pre-rRNA processing, pre-rRNA methylation, and ribosome assembly. Cell 72:443-457.
53. Trachsel, H. 1996. Binding of initiator methionyl-tRNA to ribosomes, p. 113-138. In J. W. B. Hershey, M. B. Mathews, and N. Sonenberg (ed.), Translational control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
54. 1 complex, is homologous to a gene implicated in eukaryotic cell differentiation. J. Biol. Chem. 270:9961-9970.
55. Voss, H., J. Tamanes, C. Teodoru, A. Valencia, C. Sensen, S. Wiemann, C. Schwager, J. Zimmermann, C. Sander, and W. Ansorge. 1995. Nucleotide sequence and analysis of the centromeric region of yeast chromosome IX. Yeast 11:61-78.
56. Wahle, E., and W. Keller. 1992. The biochemistry of 3′-end cleavage and polyadenylation of messenger RNA precursors. Annu. Rev. Biochem. 61: 419-440.
57. Warner, J. R. 1990. The nucleolus and ribosome formation. Curr. Opin. Cell Biol. 2:521-527.
58. Wise, J. A. 1991. Preparation and analysis of low molecular weight RNAs and small ribonucleoproteins. Methods Enzymol. 194:405-411.
59. Woolford, J. L. 1991. The structure and biogenesis of yeast ribosomes. Adv. Genet. 29:63-118.
60. Zinker, S., and J. R. Warner. 1976. The ribosomal proteins at Saccharomyces cerevisiae. J. Biol. Chem. 251:1799-1807.